3V97
Crystal structure of bifunctional methyltransferase YcbY (RlmLK) from Escherichia coli, SAH binding
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL17U |
Synchrotron site | SSRF |
Beamline | BL17U |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-11-01 |
Detector | MARMOSAIC 225 mm CCD |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 73.646, 140.834, 102.866 |
Unit cell angles | 90.00, 102.30, 90.00 |
Refinement procedure
Resolution | 49.910 - 2.200 |
R-factor | 0.18877 |
Rwork | 0.186 |
R-free | 0.23392 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2b78 3ldg 3ldf |
RMSD bond length | 0.023 |
RMSD bond angle | 2.191 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | |
High resolution limit [Å] | 2.200 | 2.200 |
Number of reflections | 99787 | |
Completeness [%] | 96.8 | 96.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7 | 289 | 0.1M HEPES, 12%(w/v) PEG8000, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 289K |